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Protein

Arachidonate 15-lipoxygenase

Gene

ALOX15

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators. Converts arachidonic acid into 12-hydroperoxyeicosatetraenoic acid/12-HPETE and 15-hydroperoxyeicosatetraenoic acid/15-HPETE. Also converts linoleic acid to 13-hydroperoxyoctadecadienoic acid. May also act on (12S)-hydroperoxyeicosatetraenoic acid/(12S)-HPETE to produce hepoxilin A3. Probably plays an important role in the immune and inflammatory responses. Through the oxygenation of membrane-bound phosphatidylethanolamine in macrophages may favor clearance of apoptotic cells during inflammation by resident macrophages and prevent an autoimmune response associated with the clearance of apoptotic cells by inflammatory monocytes. In parallel, may regulate actin polymerization which is crucial for several biological processes, including macrophage function. May also regulate macrophage function through regulation of the peroxisome proliferator activated receptor signaling pathway. Finally, it is also involved in the cellular response to IL13/interleukin-13. In addition to its role in the immune and inflammatory responses, may play a role in epithelial wound healing in the cornea maybe through production of lipoxin A4. May also play a role in endoplasmic reticulum stress response and the regulation of bone mass.2 Publications

Catalytic activityi

Arachidonate + O2 = (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate.
Arachidonate + O2 = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate.

Cofactori

Fe cationPROSITE-ProRule annotationNote: Binds 1 Fe cation per subunit.PROSITE-ProRule annotation

Enzyme regulationi

Activity is increased by binding phosphatidylinositol phosphates, especially phosphatidylinositol 3,4-bisphosphate and phosphatidylinositol 4,5-bisphosphate.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi360 – 3601Iron; catalyticPROSITE-ProRule annotation
Metal bindingi365 – 3651Iron; catalyticPROSITE-ProRule annotation
Metal bindingi540 – 5401Iron; catalyticPROSITE-ProRule annotation
Metal bindingi544 – 5441Iron; catalyticPROSITE-ProRule annotation
Metal bindingi662 – 6621Iron; via carboxylate; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

  1. arachidonate 12-lipoxygenase activity Source: UniProtKB
  2. arachidonate 15-lipoxygenase activity Source: UniProtKB
  3. eoxin A4 synthase activity Source: Reactome
  4. hepoxilin A3 synthase activity Source: Ensembl
  5. hepoxilin-epoxide hydrolase activity Source: Ensembl
  6. iron ion binding Source: UniProtKB
  7. phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB

GO - Biological processi

  1. apoptotic cell clearance Source: UniProtKB
  2. arachidonic acid metabolic process Source: UniProtKB
  3. bone mineralization Source: UniProtKB
  4. cellular response to calcium ion Source: UniProtKB
  5. cellular response to interleukin-13 Source: UniProtKB
  6. hepoxilin biosynthetic process Source: UniProtKB
  7. inflammatory response Source: ProtInc
  8. leukotriene metabolic process Source: Reactome
  9. lipoxin A4 biosynthetic process Source: UniProtKB
  10. lipoxygenase pathway Source: UniProtKB
  11. negative regulation of adaptive immune response Source: UniProtKB
  12. ossification Source: UniProtKB
  13. phosphatidylethanolamine biosynthetic process Source: UniProtKB
  14. positive regulation of actin filament polymerization Source: UniProtKB
  15. positive regulation of cell-substrate adhesion Source: UniProtKB
  16. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  17. positive regulation of heterotypic cell-cell adhesion Source: Ensembl
  18. regulation of engulfment of apoptotic cell Source: UniProtKB
  19. regulation of peroxisome proliferator activated receptor signaling pathway Source: UniProtKB
  20. response to endoplasmic reticulum stress Source: UniProtKB
  21. small molecule metabolic process Source: Reactome
  22. wound healing Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

Calcium, Iron, Lipid-binding, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS08621-MONOMER.
BRENDAi1.13.11.33. 2681.
ReactomeiREACT_150201. Synthesis of 12-eicosatetraenoic acid derivatives.
REACT_150420. Synthesis of Leukotrienes (LT) and Eoxins (EX).
REACT_150422. Synthesis of 15-eicosatetraenoic acid derivatives.
UniPathwayiUPA00881.

Names & Taxonomyi

Protein namesi
Recommended name:
Arachidonate 15-lipoxygenase (EC:1.13.11.33)
Short name:
15-LOX
Short name:
15-LOX-1
Alternative name(s):
12/15-lipoxygenase
Arachidonate 12-lipoxygenase, leukocyte-type (EC:1.13.11.31)
Short name:
12-LOX
Arachidonate omega-6 lipoxygenase
Gene namesi
Name:ALOX15
Synonyms:LOG15
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:433. ALOX15.

Subcellular locationi

Cytoplasmcytosol. Cell membrane; Peripheral membrane protein. Lipid droplet
Note: Predominantly cytosolic; becomes enriched at membranes upon calcium binding. Translocates from the cytosol to the plasma membrane when stimulated by IL13/interleukin-13 and in macrophages binding apoptotic cells.

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  3. lipid particle Source: UniProtKB
  4. membrane Source: UniProtKB
  5. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Lipid droplet, Membrane

Pathology & Biotechi

Involvement in diseasei

Disease susceptibility may be associated with variations affecting the gene represented in this entry. Met at position 560 may confer interindividual susceptibility to coronary artery disease (CAD) (PubMed:17959182).

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi418 – 4181M → V: Catalyzes 15- and 12-lipoxygenation. 1 Publication

Organism-specific databases

PharmGKBiPA48.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 662661Arachidonate 15-lipoxygenasePRO_0000220697Add
BLAST

Proteomic databases

PaxDbiP16050.
PRIDEiP16050.

PTM databases

PhosphoSiteiP16050.

Expressioni

Tissue specificityi

Detected in monocytes and eosinophils (at protein level). Expressed in airway epithelial cells.2 Publications

Inductioni

Up-regulated by UV-irradiation.1 Publication

Gene expression databases

BgeeiP16050.
CleanExiHS_ALOX15.
ExpressionAtlasiP16050. baseline and differential.
GenevestigatoriP16050.

Organism-specific databases

HPAiCAB004962.
CAB004963.
HPA013859.

Interactioni

Subunit structurei

Interacts with PEBP1; in response to IL13/interleukin-13, prevents the interaction of PEBP1 with RAF1 to activate the ERK signaling cascade.1 Publication

Protein-protein interaction databases

BioGridi106747. 1 interaction.
DIPiDIP-60388N.
STRINGi9606.ENSP00000293761.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ABTmodel-A2-662[»]
SMRiP16050. Positions 2-662.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 114113PLATPROSITE-ProRule annotationAdd
BLAST
Domaini115 – 662548LipoxygenasePROSITE-ProRule annotationAdd
BLAST

Domaini

The PLAT domain can bind calcium ions; this promotes association with membranes.By similarity

Sequence similaritiesi

Belongs to the lipoxygenase family.Curated
Contains 1 lipoxygenase domain.PROSITE-ProRule annotation
Contains 1 PLAT domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG133298.
GeneTreeiENSGT00550000074415.
HOVERGENiHBG005150.
InParanoidiP16050.
KOiK00460.
OrthoDBiEOG7B05CG.
PhylomeDBiP16050.
TreeFamiTF105320.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
InterProiIPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001885. LipOase_mml.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERiPTHR11771. PTHR11771. 1 hit.
PfamiPF00305. Lipoxygenase. 2 hits.
PF01477. PLAT. 1 hit.
[Graphical view]
PRINTSiPR00087. LIPOXYGENASE.
PR00467. MAMLPOXGNASE.
SMARTiSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMiSSF48484. SSF48484. 1 hit.
SSF49723. SSF49723. 1 hit.
PROSITEiPS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P16050-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGLYRIRVST GASLYAGSNN QVQLWLVGQH GEAALGKRLW PARGKETELK
60 70 80 90 100
VEVPEYLGPL LFVKLRKRHL LKDDAWFCNW ISVQGPGAGD EVRFPCYRWV
110 120 130 140 150
EGNGVLSLPE GTGRTVGEDP QGLFQKHREE ELEERRKLYR WGNWKDGLIL
160 170 180 190 200
NMAGAKLYDL PVDERFLEDK RVDFEVSLAK GLADLAIKDS LNVLTCWKDL
210 220 230 240 250
DDFNRIFWCG QSKLAERVRD SWKEDALFGY QFLNGANPVV LRRSAHLPAR
260 270 280 290 300
LVFPPGMEEL QAQLEKELEG GTLFEADFSL LDGIKANVIL CSQQHLAAPL
310 320 330 340 350
VMLKLQPDGK LLPMVIQLQL PRTGSPPPPL FLPTDPPMAW LLAKCWVRSS
360 370 380 390 400
DFQLHELQSH LLRGHLMAEV IVVATMRCLP SIHPIFKLII PHLRYTLEIN
410 420 430 440 450
VRARTGLVSD MGIFDQIMST GGGGHVQLLK QAGAFLTYSS FCPPDDLADR
460 470 480 490 500
GLLGVKSSFY AQDALRLWEI IYRYVEGIVS LHYKTDVAVK DDPELQTWCR
510 520 530 540 550
EITEIGLQGA QDRGFPVSLQ ARDQVCHFVT MCIFTCTGQH ASVHLGQLDW
560 570 580 590 600
YSWVPNAPCT MRLPPPTTKD ATLETVMATL PNFHQASLQM SITWQLGRRQ
610 620 630 640 650
PVMVAVGQHE EEYFSGPEPK AVLKKFREEL AALDKEIEIR NAKLDMPYEY
660
LRPSVVENSV AI
Length:662
Mass (Da):74,804
Last modified:January 23, 2007 - v3
Checksum:i9ACF7FE7863A045C
GO
Isoform 2 (identifier: P16050-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     46-84: Missing.

Note: No experimental confirmation available.

Show »
Length:623
Mass (Da):70,108
Checksum:i71B99C6D8E707189
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti46 – 461E → V in AAC52118 (PubMed:9700053).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti90 – 901D → H.1 Publication
Corresponds to variant rs11568142 [ dbSNP | Ensembl ].
VAR_018746
Natural varianti102 – 1021G → V.
Corresponds to variant rs41439950 [ dbSNP | Ensembl ].
VAR_035036
Natural varianti103 – 1031N → K.1 Publication
Corresponds to variant rs11568099 [ dbSNP | Ensembl ].
VAR_018747
Natural varianti205 – 2051R → Q.1 Publication
Corresponds to variant rs11568101 [ dbSNP | Ensembl ].
VAR_018748
Natural varianti239 – 2391V → M.
Corresponds to variant rs3892408 [ dbSNP | Ensembl ].
VAR_035037
Natural varianti461 – 4611A → P.1 Publication
Corresponds to variant rs17852628 [ dbSNP | Ensembl ].
VAR_035038
Natural varianti560 – 5601T → M Loss of catalytic activity. 1 Publication
Corresponds to variant rs34210653 [ dbSNP | Ensembl ].
VAR_035039

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei46 – 8439Missing in isoform 2. 1 PublicationVSP_056681Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23892 mRNA. Translation: AAA36182.1.
U88317 Genomic DNA. Translation: AAB49305.1.
AK290309 mRNA. Translation: BAF82998.1.
AK316126 mRNA. Translation: BAH14497.1.
AY505111 Genomic DNA. Translation: AAR84235.1.
AC118754 Genomic DNA. No translation available.
BC029032 mRNA. Translation: AAH29032.1.
U63384 Genomic DNA. Translation: AAC52118.1.
CCDSiCCDS11049.1. [P16050-1]
PIRiA31349.
RefSeqiNP_001131.3. NM_001140.3. [P16050-1]
UniGeneiHs.73809.

Genome annotation databases

EnsembliENST00000293761; ENSP00000293761; ENSG00000161905. [P16050-1]
ENST00000570836; ENSP00000458832; ENSG00000161905. [P16050-1]
ENST00000574640; ENSP00000460483; ENSG00000161905. [P16050-2]
GeneIDi246.
KEGGihsa:246.
UCSCiuc002fyh.3. human. [P16050-1]

Polymorphism databases

DMDMi126396.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23892 mRNA. Translation: AAA36182.1.
U88317 Genomic DNA. Translation: AAB49305.1.
AK290309 mRNA. Translation: BAF82998.1.
AK316126 mRNA. Translation: BAH14497.1.
AY505111 Genomic DNA. Translation: AAR84235.1.
AC118754 Genomic DNA. No translation available.
BC029032 mRNA. Translation: AAH29032.1.
U63384 Genomic DNA. Translation: AAC52118.1.
CCDSiCCDS11049.1. [P16050-1]
PIRiA31349.
RefSeqiNP_001131.3. NM_001140.3. [P16050-1]
UniGeneiHs.73809.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ABTmodel-A2-662[»]
SMRiP16050. Positions 2-662.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106747. 1 interaction.
DIPiDIP-60388N.
STRINGi9606.ENSP00000293761.

Chemistry

BindingDBiP16050.
ChEMBLiCHEMBL2903.

PTM databases

PhosphoSiteiP16050.

Polymorphism databases

DMDMi126396.

Proteomic databases

PaxDbiP16050.
PRIDEiP16050.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000293761; ENSP00000293761; ENSG00000161905. [P16050-1]
ENST00000570836; ENSP00000458832; ENSG00000161905. [P16050-1]
ENST00000574640; ENSP00000460483; ENSG00000161905. [P16050-2]
GeneIDi246.
KEGGihsa:246.
UCSCiuc002fyh.3. human. [P16050-1]

Organism-specific databases

CTDi246.
GeneCardsiGC17M004534.
HGNCiHGNC:433. ALOX15.
HPAiCAB004962.
CAB004963.
HPA013859.
MIMi152392. gene.
neXtProtiNX_P16050.
PharmGKBiPA48.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG133298.
GeneTreeiENSGT00550000074415.
HOVERGENiHBG005150.
InParanoidiP16050.
KOiK00460.
OrthoDBiEOG7B05CG.
PhylomeDBiP16050.
TreeFamiTF105320.

Enzyme and pathway databases

UniPathwayiUPA00881.
BioCyciMetaCyc:HS08621-MONOMER.
BRENDAi1.13.11.33. 2681.
ReactomeiREACT_150201. Synthesis of 12-eicosatetraenoic acid derivatives.
REACT_150420. Synthesis of Leukotrienes (LT) and Eoxins (EX).
REACT_150422. Synthesis of 15-eicosatetraenoic acid derivatives.

Miscellaneous databases

GeneWikiiALOX15.
GenomeRNAii246.
NextBioi35480819.
PROiP16050.
SOURCEiSearch...

Gene expression databases

BgeeiP16050.
CleanExiHS_ALOX15.
ExpressionAtlasiP16050. baseline and differential.
GenevestigatoriP16050.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
InterProiIPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001885. LipOase_mml.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERiPTHR11771. PTHR11771. 1 hit.
PfamiPF00305. Lipoxygenase. 2 hits.
PF01477. PLAT. 1 hit.
[Graphical view]
PRINTSiPR00087. LIPOXYGENASE.
PR00467. MAMLPOXGNASE.
SMARTiSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMiSSF48484. SSF48484. 1 hit.
SSF49723. SSF49723. 1 hit.
PROSITEiPS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
  2. "Characterization and sequence of an additional 15-lipoxygenase transcript and of the human gene."
    Kritzik M.R., Ziober A.F., Dicharry S., Conrad D.J., Sigal E.
    Biochim. Biophys. Acta 1352:267-281(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Tongue.
  4. SeattleSNPs variation discovery resource
    Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-90; LYS-103 AND GLN-205.
  5. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT PRO-461.
    Tissue: Brain and Lung.
  7. "Human 15-lipoxygenase gene promoter: analysis and identification of DNA binding sites for IL-13-induced regulatory factors in monocytes."
    Kelavkar U., Wang S., Montero A., Murtagh J., Shah K., Badr K.
    Mol. Biol. Rep. 25:173-182(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-46.
  8. "Arachidonate 15-lipoxygenase (omega-6 lipoxygenase) from human leukocytes. Purification and structural homology to other mammalian lipoxygenases."
    Sigal E., Grunberger D., Craik C.S., Caughey G.H., Nadel J.A.
    J. Biol. Chem. 263:5328-5332(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-16.
  9. "Purification of two forms of arachidonate 15-lipoxygenase from human leukocytes."
    Izumi T., Raadmark O., Joernvall H., Samuelsson B.
    Eur. J. Biochem. 202:1231-1238(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-31; 38-45; 157-168 AND 626-631.
    Tissue: Eosinophil and Leukocyte.
  10. "A primary determinant for lipoxygenase positional specificity."
    Sloane D.L., Leung R., Craik C.S., Sigal E.
    Nature 354:149-152(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF MET-418.
  11. "Membrane translocation of 15-lipoxygenase in hematopoietic cells is calcium-dependent and activates the oxygenase activity of the enzyme."
    Brinckmann R., Schnurr K., Heydeck D., Rosenbach T., Kolde G., Kuehn H.
    Blood 91:64-74(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  12. "Evaluation of the activity and localization of 15-lipoxygenase-1 after introduction into human colorectal carcinoma Caco-2 cells."
    Hsi L.C., Kamitani H., Cornicelli J.A., Eling T.E.
    Prostaglandins Leukot. Essent. Fatty Acids 64:217-225(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  13. "Interaction of human 15-lipoxygenase-1 with phosphatidylinositol bisphosphates results in increased enzyme activity."
    Andersson E., Schain F., Svedling M., Claesson H.E., Forsell P.K.
    Biochim. Biophys. Acta 1761:1498-1505(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: LIPID-BINDING, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, FUNCTION, ENZYME REGULATION.
  14. "Reciprocal regulation of 12- and 15-lipoxygenases by UV-irradiation in human keratinocytes."
    Yoo H., Jeon B., Jeon M.S., Lee H., Kim T.Y.
    FEBS Lett. 582:3249-3253(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY UV.
  15. "15(S)-Lipoxygenase-1 associates with neutral lipid droplets in macrophage foam cells: evidence of lipid droplet metabolism."
    Weibel G.L., Joshi M.R., Wei C., Bates S.R., Blair I.A., Rothblat G.H.
    J. Lipid Res. 50:2371-2376(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  16. "15-Lipoxygenase 1 interacts with phosphatidylethanolamine-binding protein to regulate MAPK signaling in human airway epithelial cells."
    Zhao J., O'Donnell V.B., Balzar S., St Croix C.M., Trudeau J.B., Wenzel S.E.
    Proc. Natl. Acad. Sci. U.S.A. 108:14246-14251(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN IL13 SIGNALING, INTERACTION WITH PEBP1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  17. Cited for: VARIANT MET-560, CHARACTERIZATION OF VARIANT MET-560, INVOLVEMENT IN CORONARY ARTERY DISEASE.

Entry informationi

Entry nameiLOX15_HUMAN
AccessioniPrimary (citable) accession number: P16050
Secondary accession number(s): A8K2P4
, B7ZA11, Q8N6R7, Q99657
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 159 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.